Small-angle X-ray scattering structural insights into alternative pathway of actin oligomerization associated with inactivated state.
Biochem Biophys Res Commun
; 693: 149340, 2024 Jan 22.
Article
em En
| MEDLINE
| ID: mdl-38141525
ABSTRACT
In addition to the well-known monomeric globular (G-actin) and polymeric fibrillar (F-actin) forms, actin can exist in the so-called inactivated form (I-actin). Hsp70 chaperon, prefoldin, and CCT chaperonin are required to obtain native globular state. In contrast, I-actin is spontaneously formed in the absence of intracellular folding machinery. I-actin can be obtained from G-actin by elimination of divalent ion, incubation in presence of small concentrations of denaturants, and by heat exposure. Since G-actin is a quasi-stationary, thermodynamically unstable form, it can gradually transform into inactivated state in the absence of chelating/denaturating agents or heat exposure, but the transition is much slower. I-actin was shown to associate into oligomers up to the molecular weight of 14-16 G-actin monomers, though the structure of these oligomers remains uncharacterized. This study employs small-angle X-ray scattering to reveal novel insights into the oligomerization process of such spontaneously formed inactivated actin. These oligomers are differentiated from F-actin through comparative analysis, highlighting a unique oligomerization pathway.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Actinas
/
Dobramento de Proteína
Idioma:
En
Ano de publicação:
2024
Tipo de documento:
Article